9c86
From Proteopedia
Structure of endogenous asymmetric DPYSL2 from rat model of Alzheimer's disease
Structural highlights
FunctionDPYL2_RAT Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis (By similarity). Publication Abstract from PubMedStudying native protein structures at near-atomic resolution in a crowded environment presents challenges. Consequently, understanding the structural intricacies of proteins within pathologically affected tissues often relies on mass spectrometry and proteomic analysis. Here, we utilized cryoelectron microscopy (cryo-EM) and the Build and Retrieve (BaR) method to investigate protein complexes' structural characteristics such as post-translational modification, active site occupancy, and arrested conformational state in Alzheimer's disease (AD) using brain lysate from a rat model (TgF344-AD). Our findings reveal novel insights into the architecture of these complexes, corroborated through mass spectrometry analysis. Interestingly, it has been shown that the dysfunction of these protein complexes extends beyond AD, implicating them in cancer, as well as other neurodegenerative disorders such as Parkinson's disease, Huntington's disease, and schizophrenia. By elucidating these structural details, our work not only enhances our understanding of disease pathology but also suggests new avenues for future approaches in therapeutic intervention. Unveiling the structural proteome of an Alzheimer's disease rat brain model.,Samani EK, Hasan SMN, Waas M, Keszei AFA, Xu X, Heydari M, Hill ME, McLaurin J, Kislinger T, Mazhab-Jafari MT Structure. 2024 Nov 29:S0969-2126(24)00494-5. doi: 10.1016/j.str.2024.11.004. PMID:39615488[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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